Journal Article

PUBDB-2022-06893

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Local Flexibility of a New Single-Ring Chaperonin Encoded by Bacteriophage AR9 Bacillus subtilis

Sokolova, O. S. ; Pichkur, E. B. ; Maslova, E. S. ; Kurochkina, L. P. ; Semenyuk, P. I. ; Konarev, P. V. ; Samygina, V.Extern*EMBL* ; Stanishneva-Konovalova, T. B. (Corresponding author)

2022
MDPI Basel

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Please use a persistent id in citations: doi:10.3390/biomedicines10102347  doi:10.3204/PUBDB-2022-06893

Abstract: Chaperonins, a family of molecular chaperones, assist protein folding in all domains of life. They are classified into two groups: bacterial variants and those present in endosymbiotic organelles of eukaryotes belong to group I, while group II includes chaperonins from the cytosol of archaea and eukaryotes. Recently, chaperonins of a prospective new group were discovered in giant bacteriophages; however, structures have been determined for only two of them. Here, using cryo-EM, we resolved a structure of a new chaperonin encoded by gene 228 of phage AR9 B. subtilis. This structure has similarities and differences with members of both groups, as well as with other known phage chaperonins, which further proves their diversity.

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Contributing Institute(s):

1. EMBL-User (EMBL-User)

Research Program(s):

1. 6G3 - PETRA III (DESY) (POF4-6G3) (POF4-6G3)

Experiment(s):

1. PETRA Beamline P12 (PETRA III)

Appears in the scientific report 2022

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